entryaccgenealt_geneolnprotein_namecm_locacm_notescm_refssuboci_fullsublocisubloci_iimnterm_ctermbernselsubloci_uniprotsubloci_echoLorganelletarget_chaperoning11st_sstarget_chaperoning22nd_sspseudocommon_corebasic_proteomesignalp_sp_existsignalp_possignalp_cmaxlipop_predlipop_cleavagelipop_scorelipop_ruletmhmmphobius_tmsphobius_sp_existphobius_predictionpsortb_locapsortb_scoresolubility
YMGJ_ECOLIA5A612
ymgJ
b4594 periplasmic protein (SEC through IM), YmgJWeak signal peptide prediction. Function Unkown.PeriplasmicGIM (predicted)-SECnoyesN240.144CYT0-0.200913-00Yn6-17c22/23oUnknown2
SODM_ECOLIP00448
sodA
b3908 JW3879 periplasmic protein (SEC through IM), Superoxide dismutase SodAPeriplasmicThe superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism in Rhizobium leguminosarum. SodM and SodF are <i>E.coli</i> proteins that are close homoloques of the RISodA. SodA does not possess a hydrophobic cleaved N-terminal signal peptide typically present in soluble proteins exported by the Sec-dependent (Sec) pathway or the twin-arginine translocation (TAT) pathway. TatC or SecB mutants in Rhizobium leguminosarum do not affect export of SodA to the periplasm. Inhibition of SecA ATPase activity by azide blocks SodA export to the periplasm.PMID: 21854464PeriplasmicGN/ACytoplasmicSECyesyesN510.145CYT0-0.200913-00NiUnknown5
ENO_ECOLIP0A6P9
eno
b2779 JW2750 cytoplasmic peripheral IM protein facing the cytoplasm & peripheral OM protein facing the extra-cellular space (SEC through IM), Enolase EnoCytoplasmic, Peripheral inner membrane protein facing the cytoplasm, Peripheral outer membrane protein facing the extra-cellular spaceWhen modified at Lys342 possibly secreted by an unknown mechanism, no evidence of signal peptide) Homodimer, stabilized by Mg2+; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. Essential for the degradation of carbohydrates via glycolysis. Also a component of the RNA degradosome. The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Interacts with the C-terminal region of the endoribonuclease RNase EIn the RNA degradosome. Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm,Is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the bacterial cell surface. PMID: 8610017 PMID: 9600841 PMID: 9740056 PMID: 9732527 PMID: 12035760 Detected in acossiation with the inner membrane (sequential biochemical fractionations coupled with high resolution mass spectrometry). PMID: 23230279PMID: 12035760 PMID: 15003462 PMID: 17242352 PMID: 18337249 PMID: 23230279 PMID: 8610017 PMID: 9600841 PMID: 9732527 PMID: 9740056Cytoplasmic, Peripheral inner membrane protein facing the cytoplasm, Peripheral outer membrane protein facing the extra-cellular spaceA, F1, F4Soluble IM FractionCytoplasm; cytoskeleton Secreted Cell surface Cytoplasmic (Experimental)SECyesyesN420.139CYT0-0.200913-00NiCytoplasmic9100
YGFZ_ECOLIP0ADE8
ygfZ

yzzW

yzzWb2898 JW2866 cytoplasmic & periplasmic protein (SEC through IM), tRNA-modifying YgfZ Cytoplasmic, PeriplasmicSubcellular localization analysis of cytotoxic necrotizing factor 1 <a href="http://www.uniprot.org/uniprot/Q1R2U0">(CNF1)</a> demonstrated that YgfZ, a periplasmic protein, contributes to secretion of CNF1 (a normally cytoplasmic protein) into outer-membrane vesicles (OMVs) in pathogenic E.coli strain RS218 O18:K1:H7 PMID: 22174383. PMID: 9298646PMID: 22174383 PMID: 9298646Cytoplasmic, PeriplasmicA, GN/ACytoplasm Cytoplasmic (Experimental)SECyesyesN310.252CYT0-0.200913-00NiUnknown282
FTSL_ECOLIP0AEN4
ftsL

mraR yabD

mraR yabDb0083 JW0081 IM lipoprotein (SEC through IM), Cell division FtsLInner Membrane LipoproteinLocalizes to potential division sites in filamentous cells. Proven pignal peptidase II substrate. PMID: 1332942PMID: 10027987 PMID: 11703663 PMID: 11948172 PMID: 1332942 PMID: 15165235 PMID: 15174130 PMID: 21890895Inner Membrane LipoproteinEIM (predicted)Cell inner membrane Membrane anchored (Experimental)SECyesyesN240.167CYT0-0.200913-11No35-57iCytoplasmic825
SODF_ECOLIP0AGD3
sodB
b1656 JW1648 periplasmic protein (SEC through IM), Superoxide dismutase SodBPeriplasmicThe superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism in Rhizobium leguminosarum. SodM and SodF are <i>E.coli</i> proteins that are close homoloques of the RISodA. SodA does not possess a hydrophobic cleaved N-terminal signal peptide typically present in soluble proteins exported by the Sec-dependent (Sec) pathway or the twin-arginine translocation (TAT) pathway. TatC or SecB mutants in Rhizobium leguminosarum do not affect export of SodA to the periplasm. Inhibition of SecA ATPase activity by azide blocks SodA export to the periplasm.PeriplasmicGN/ACytoplasmicSECyesyesN170.122CYT0-0.200913-00NiPeriplasmic977
PNCB_ECOLIP18133
pncB
b0931 JW0914 periplasmic protein (SEC through IM), Nicotinate phosphoribosyltransferase PncBPeriplasmicPncB is localized in the periplasm although it does not possess a signal peptide.PMID: 346557PeriplasmicGN/ACytoplasmicSECnoyesN610.11CYT0-0.200913-00NiCytoplasmic932
SPEA_ECOLIP21170
speA
b2938 JW2905 periplasmic protein (SEC through IM), Biosynthetic arginine decarboxylase SpeAPeriplasmicTrigger factor-sensitive aggregation. Experimentally detected by proteomics analysis of E.coli membrane fraction PMID: 19766000. No transmembrane helix is predicted. Weak hydrophobic and non cytoplasmic regions predicted by Phobius. Potential peripherally associated protein facing the cytoplasm or integral inner membrane protein. PMID: 2198270 Selective disruption of the cell envelope and an assessment of Spea activity or immunoprecipitable SpeA in various fractions demonstrated its location between the cytoplasmic membrane and peptidoglycan layer. PMID: 3894328PMID: 15919657 PMID: 19737520 PMID: 19766000 PMID: 2198270 PMID: 3894328PeriplasmicGSoluble IM FractionPeriplasm CytoplasmicTFSECyesyesN270.129CYT0-0.200913-00NiPeriplasmic1048
EAEH_ECOLIP36943
eaeH
b0297 JW0291 periplasmic protein (SEC through IM), Putative attaching and effacing homolog EaeHPeriplasmicUniprot gives portential signal peptide (1-25) although it is not predicted by any tool. Intimin homologue but missing the C-terminus. Intimin is in the OM. Could be periplasmic. The signal peptide could be long autotransporter-like signal peptide. Intimin does not have a classical signal peptide either. PeriplasmicGN/AMembrane anchoredSECpseudogene (Uniprot), pseudogene (Ochman & Davalos, 2006)nonoN450.383CYT0-0.200913-11Ni21-44oOuterMembrane95
YIAD_ECOLIP37665
yiaD
b3552 JW5657 OM lipoprotein (SEC through IM), inserted in OM by LOL), Probable YiaDOuter Membrane Lipoprotein Proven pignal peptidase II substrate. PMID: 15174130PMID: 15174130 PMID: 15919996 PMID: 20932056Outer Membrane LipoproteinIout/outN/ACell inner membrane Outer membrane Lipoprotein (Experimental)SECLOLyesyesY180.162SpII2021.9879Pos+2=T32Yn5-16c20/21o36-55i62-81oOuterMembrane1063
RMLA1_ECOLIP37744
rfbA

rmlA rmlA1

rmlA rmlA1b2039 JW2024 periplasmic protein (SEC through IM), Glucose-1-phosphate thymidylyltransferase 1 RfbAPeriplasmicPMID: 23138692 PMID: 7537247PeriplasmicGIM (predicted-detected)CytoplasmicSECyesyesN240.125CYT0-0.200913-00Yn7-18c23/24oCytoplasmic963
YCGI_ECOLIP76000
ycgI

ymgH

ymgHb4521 JW1162/JW5179 b1173OM b-barrel protein (SEC through IM), T5S secreted through OM), Putative YcgIContains a predicted autotransporter domain. Potential outer membrane b-barrel protein though it does not have prediction for a signal peptide. Contains autotransporter beta-domain <a href="http://www.ebi.ac.uk/interpro/entry/IPR005546/proteins-matched?species=83333">(IPR005546)</a>Outer Membrane b-barrel proteinHN/ACytoplasmicSECAutotransporter(T5S)pseudogene (Uniprot), pseudogene (Ochman & Davalos, 2006)nonoN250.12CYT0-0.200913-00NiUnknown712
YCGV_ECOLIP76017
ycgV
b1202 JW1193 OM b-barrel protein (SEC through IM, T5S secreted through OM), YcgVOuter Membrane b-barrel proteinAg43 homologue; known autotransporter protein. Signal peptide 1-56 (by clustalW). Contains autotransporter beta-domain <a href="http://www.ebi.ac.uk/interpro/entry/IPR005546/proteins-matched?species=83333">(IPR005546)</a>. Potential Srp-dependent autotransporter. Homologous to hemoglobin-binding protease hbp. Hbp is the only known autotransporter that is secreted through the integral membrane in a Srp-dependent manner.PMID: 12466262 PMID: 15590781Outer Membrane b-barrel proteinHIM (predicted)CytoplasmicSRPSECAutotransporter(T5S)noyesN470.309CYT0-0.200913-01Ni27-47oExtracellular917
MDTA_ECOLIP76397
mdtA

yegM

yegMb2074 JW5338 periplasmic peripheral IM protein (SEC through IM), Multidrug resistance MdtAPeripheral inner membrane protein facing the periplasmPart of MdtABC-TolC multidrug efflux transport system = [(TolC)3][MdtC][MdtB][MdtA].PMID: 12107133 PMID: 12107134 PMID: 21890895Peripheral inner membrane protein facing the periplasmF2N/ACell inner membrane Membrane anchoredSECyesyesN220.151TMH07.31567-11Ni9-26oCytoplasmicMembrane937
LOMR_ECOLIP77184
lomR
b4570 JW5884/JW5904 b1369/b1371OM b-barrel protein (SEC through IM), Putative LomROuter Membrane b-barrel proteinHN/ACytoplasmicSECInsertion Sequence, pseudogene (Uniprot), pseudogene (Ochman & Davalos, 2006)nonoN270.169SpI260.733275-00NiOuterMembrane10
YDEU_ECOLIP77286
ydeU
b1509 JW1502 OM b-barrel protein (SEC through IM, T5S secreted through OM), YdeUOuter Membrane b-barrel proteinAg43 homologue; predicted autotransporter.PMID: 15590781Outer Membrane b-barrel proteinHN/ACytoplasmicSECAutotransporter(T5S)pseudogene (Uniprot)noyesN330.107CYT0-0.200913-00NiOuterMembrane93
HLYE_ECOLIP77335
hlyE

clyA hpr sheA ycgD

clyA hpr sheA ycgDb1182 JW5181 periplasmic & extra-cellular protein (SEC through IM), secreted in OMV), Hemolysin E, chromosomal HlyEPeriplasmic, Extra-cellularHlyE(ClyA) forms a dodecameric transmembrane pore. The ability of ClyA to translocate to the periplasm is abolished in deletion mutants lacking the last 23 or 11 amino acid residues of the C-terminal region. Also, analysis of ClyA mutants with defined deletions and amino acid exchanges revealed that several ClyA segments which are distant of each other in the primary structure, namely, the N-terminal ??A1 region, the C-terminal region, and the hydrophobic sequence ranging from residues 89 to 101, are crucial for ClyA translocation from the E. coli cytoplasm to the periplasm. In the soluble ClyA monomer, these regions are found closely adjacent to each other in the tail domain. ClyA assembles into an oligomeric structure in solution in the absence of either bilayer membranes or detergents at physiological temperature.These oligomers can rearrange to create transmembrane pores when in contact with detergents or biological membranes. ClyA does not form transmembrane pores on E. coli lipid membranes. Recombinant E. coli overexpressing the cloned clyA gene accumulated this haemolysin in the periplasm and released only very small amounts of it into the external medium. PMID: 11902713 Disulfide bridge (87 285) PMID: 14532000PMID: 10027972 PMID: 11902713 PMID: 14532000 PMID: 19421192 PMID: 20511497 PMID: 24019520 PMCID: PMC2916382Periplasmic, Extra-cellularG, XN/ASecreted Periplasm Host cell membrane Secreted and released (Experimental)SECOMVnoyesN580.117CYT0-0.200913-10NiExtracellular1062
YAFY_ECOLIP77365
yafY
b0251 JW0240 IM lipoprotein (SEC through IM, inserted in OM by LOL), YafYInner Membrane LipoproteinPMID: 23138451Inner Membrane LipoproteinEN/ACell inner membrane CytoplasmicSECLOLProphage Integrase (EcoGene)nonoY210.302SpII2017.0831Pos+2=D00Yn6-17c21/22oUnknown227